ATP-dependent DNA helicase PIF1

Definition:

DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Possesses an intrinsic strand annealing activity.

References:

[1]. Kazunobu Futami, et al. Mitochondrial and nuclear localization of human Pif1 helicase. Biol Pharm Bull. 2007 Sep;30(9):1685-92. [Content Brief]

[2]. Katrin Paeschke, et al. Pif1 family helicases suppress genome instability at G-quadruplex motifs. Nature. 2013 May 23;497(7450):458-62. [Content Brief]

[3]. Maria K Mateyak, et al. Human PIF helicase is cell cycle regulated and associates with telomerase. Cell Cycle. 2006 Dec;5(23):2796-804. [Content Brief]

[4]. Yongqing Gu, et al. Biochemical analysis of human PIF1 helicase and functions of its N-terminal domain. Nucleic Acids Res. 2008 Nov;36(19):6295-308. [Content Brief]

[5]. Tresa George, et al. Human Pif1 helicase unwinds synthetic DNA structures resembling stalled DNA replication forks. Nucleic Acids Res. 2009 Oct;37(19):6491-502. [Content Brief]

[6]. Cyril M Sanders, et al. Human Pif1 helicase is a G-quadruplex DNA-binding protein with G-quadruplex DNA-unwinding activity. Biochem J. 2010 Aug 15;430(1):119-28. [Content Brief]

[7]. Deng-Hong Zhang, et al. The human Pif1 helicase, a potential Escherichia coli RecD homologue, inhibits telomerase activity. Nucleic Acids Res. 2006 Mar 6;34(5):1393-404. [Content Brief]

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